1F45: Human interleukin-12

Human interleukin-12. Determined by X-ray diffraction at 2.8 Å resolution. Released 20 Jun 2001.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,348
Mol. weight: 57.89 kDa
Released: 20 Jun 2001

Explore 1F45 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F45 contains 12 α-helices and 33 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	1
β-strand	8-14	7	1
β-strand	22-24	3	2
β-strand	27	1	3
β-strand	37-38	2	4
β-strand	39-40	2	5
β-strand	48-49	2	4
β-strand	52	1	3
β-strand	55-57	3	2
α-helix	60-62	3
β-strand	65	1	1
β-strand	66-67	2	5
β-strand	79-86	8	1
β-strand	89-90	2	1
β-strand	108-110	3	6
β-strand	111	1	7
β-strand	117-124	8	6
β-strand	131-138	8	1
β-strand	145	1	1
β-strand	146-148	3	6
β-strand	152-155	4	6
β-strand	165-173	9	6
α-helix	180-182	3
β-strand	186-194	9	1
β-strand	197-205	9	1
α-helix	207-209	3
β-strand	211	1	7
α-helix	213-216	4
β-strand	217-220	4	8
β-strand	229-235	7	8
β-strand	249-255	7	9
β-strand	266-269	4	9
β-strand	273-277	5	8
β-strand	284-290	7	9
α-helix	296-300	5
β-strand	301-303	3	9

Chain B: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	21-36	16
α-helix	37-39	3
α-helix	59-62	4
β-strand	65	1	10
α-helix	66-70	5
β-strand	82	1	10
α-helix	96-123	28
α-helix	133-147	15
α-helix	168-195	28

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interleukin-12 beta chain	A	protein	306	Homo sapiens	P29460 (AlphaFold model)
Interleukin-12 alpha chain	B	protein	197	Homo sapiens	P29459 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1F45_1 INTERLEUKIN-12 BETA CHAIN (chains A)
IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEF
GDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTC
WWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAA
EESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTW
STPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEW
ASVPCS

Sequence of entity 2 (B), FASTA

>1F45_2 INTERLEUKIN-12 ALPHA CHAIN (chains B)
RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTV
EACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMN
AKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAF
RIRAVTIDRVMSYLNAS

Primary citation

Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12. Yoon, C., Johnston, S.C., Tang, J. et al. EMBO J (2000) 19:3530-3541. DOI 10.1093/emboj/19.14.3530 · PubMed

Other PDB entries of the same protein (UniProt P29460 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5MJ3 1.74 Å, Interleukin-23 complex with an antagonistic alphabody, crystal form 1
3D85 1.9 Å, Crystal structure of IL-23 in complex with neutralizing FAB
8CR8 2.0 Å, human Interleukin-23
3DUH 2.3 Å, Structure of Interleukin-23
8UUI 2.43 Å, X-ray structure of Interleukin-23 in complex with peptide 23-446
1F42 2.5 Å, The P40 domain of human interleukin-12
5MXA 2.5 Å, Structure of unbound Interleukin-23
4GRW 2.55 Å, Structure of a complex of human IL-23 with 3 Nanobodies (Llama vHHs)
6UIB 2.74 Å, Crystal structure of IL23 bound to peptide 23-652
5MZV 2.8 Å, IL-23:IL-23R:Nb22E11 complex
3D87 2.9 Å, Crystal structure of Interleukin-23
3HMX 3.0 Å, Crystal structure of ustekinumab FAB/IL-12 complex

Browse structure collections

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